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  • 2000-2004  (3)
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  • 2000-2004  (3)
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  • 1
    Online Resource
    Online Resource
    Identification of a pH regulated Na + /H + antiporter of Methanococcus jannaschii
    Wiley ; 2002
    In:  FEBS Letters Vol. 527, No. 1-3 ( 2002-09-11), p. 245-249
    Details
    In: FEBS Letters, Wiley, Vol. 527, No. 1-3 ( 2002-09-11), p. 245-249
    Abstract: The genome of the hyperthermophilic archaeon Methanococcus jannaschii contains three Na + /H + antiporter related genes Mj0057, Mj1521 and Mj1275. Comparative sequence alignments revealed that Mj0057 and Mj1521 belong to the NhaP family whereas Mj1275 is a member of the NapA family. The genes were cloned and expressed in the double mutant Escherichia coli strain Frag144 (ΔnhaA, ΔnhaB) to analyze their capability of mediating ΔpH driven Na + flux in everted vesicles. From the tested clones only Mj0057 displayed Na + (Li + )/H + antiporter activity. The transport was pH dependent and occurred at pH 7.0 and below. At pH 6.0 the apparent K m values for Na + and Li + were approximately 10 and 2.5 mM, respectively.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(02)03244-1
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2002
    detail.hit.zdb_id: 1460391-3
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Conserved arginine and aspartate residues are critical for function of MjNhaP1, a Na + /H + antiporter of M. jannaschii
    Wiley ; 2003
    In:  FEBS Letters Vol. 542, No. 1-3 ( 2003-05-08), p. 32-36
    Details
    In: FEBS Letters, Wiley, Vol. 542, No. 1-3 ( 2003-05-08), p. 32-36
    Abstract: Recently MjNhaP1 was identified as a pH‐regulated Na + /H + antiporter of Methanococcus jannaschii [Hellmer, J. et al. (2002) FEBS Lett. 527, 245–249]. The antiporter is active at pH 6.0 and displays continuously decreasing activity towards alkaline pH. We have performed a site‐directed mutagenesis study on all histidines as well as on conserved Asp, Glu and Arg residues of MjNhaP1, and analyzed the mutated proteins for activity. The mutants fall into three classes, i.e. normally active mutants, mutants with intermediate activity and mutants which are completely inactive. None of the histidine residues appears to be essential unlike in the bacterial proteins. The results point at an important role of a number of aspartate and arginine residues.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(03)00332-6
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2003
    detail.hit.zdb_id: 1460391-3
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
  • 3
    Online Resource
    Online Resource
    MjK1, a K + channel from M. jannaschii , mediates K + uptake and K + sensitivity in E. coli
    Wiley ; 2003
    In:  FEBS Letters Vol. 547, No. 1-3 ( 2003-07-17), p. 165-169
    Details
    In: FEBS Letters, Wiley, Vol. 547, No. 1-3 ( 2003-07-17), p. 165-169
    Abstract: The methanogenic and hyperthermophilic deep‐sea archaeon Methanococcus jannaschii has three putative K + channels, MVP (Mj0139), MjK1 (Mj0138.1) and MjK2 (Mj1357). The physiological function of these K + channels was examined in a viability assay, using the Escherichia coli mutant LB2003 (kup1, ΔkdpABC5, ΔtrkA). While MjK2 expression had no effects on the potassium‐dependent phenotype of LB2003, MVP and MjK1 complemented the deficiency at a concentration of 1 mM KCl. In contrast to KcsA, MthK and MVP, MjK1 strongly affected host cell viability at 10 and 100 mM KCl. The toxic effects were less pronounced when growth media were supplemented with the K + channel blocker BaCl 2 .
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(03)00706-3
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2003
    detail.hit.zdb_id: 1460391-3
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
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